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Article ; Online: A G₄·K⁺ hydrogel stabilized by an anion.

Peters, Gretchen Marie / Skala, Luke P / Plank, Taylor N / Hyman, Brooke J / Manjunatha Reddy, G N / Marsh, Andrew / Brown, Steven P / Davis, Jeffery T

Journal of the American Chemical Society

2014 Volume 136, Issue 36, Page(s) 12596–12599

Abstract: ... guanosine (G, 1) with 0.5 equiv of KB(OH)4. This ratio of borate anion to ligand is crucial for gelation ... as it links two molecules of 1, which facilitates cation-templated assembly of G4·K(+) quartets. The guanosine ... relevant concentrations of K(+). Furthermore, non-covalent interactions, such as electrostatics, π-stacking ...

Abstract	Supramolecular hydrogels derived from natural products have promising applications in diagnostics, drug delivery, and tissue engineering. We studied the formation of a long-lived hydrogel made by mixing guanosine (G, 1) with 0.5 equiv of KB(OH)4. This ratio of borate anion to ligand is crucial for gelation as it links two molecules of 1, which facilitates cation-templated assembly of G4·K(+) quartets. The guanosine-borate (GB) hydrogel, which was characterized by cryogenic transmission electron microscopy and circular dichroism and (11)B magic-angle-spinning NMR spectroscopy, is stable in water that contains physiologically relevant concentrations of K(+). Furthermore, non-covalent interactions, such as electrostatics, π-stacking, and hydrogen bonding, enable the incorporation of a cationic dye and nucleosides into the GB hydrogel.
MeSH term(s)	Anions/chemistry ; Borates/chemistry ; Guanosine/chemistry ; Hydrogel, Polyethylene Glycol Dimethacrylate/chemistry ; Magnetic Resonance Spectroscopy ; Molecular Structure ; Potassium/chemistry
Chemical Substances	Anions ; Borates ; Guanosine (12133JR80S) ; Hydrogel, Polyethylene Glycol Dimethacrylate (25852-47-5) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2014-09-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/ja507506c
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Article: Control of K+ channels by G proteins.

Brown, A M / Yatani, A / Kirsch, G / Okabe, K / VanDongen, A M / Birnbaumer, L

Journal of bioenergetics and biomembranes

1991 Volume 23, Issue 4, Page(s) 499–507

Abstract: ... cascade in the case of cardiac myocytes. G protein-mediated second messenger effects on K+ channels are ... established for specific G proteins and their specific K+ channel effectors. ... an hypothesis proposed in which the alpha subunits of G proteins directly couple receptors to ionic channels ...

Abstract	Heterotrimeric G3 proteins are though to couple receptors to ionic channels via cytoplasmic mediators such as cGMP in the case of retinal rods, cAMP in the case of olfactory cells, and the cAMP cascade in the case of cardiac myocytes. G protein-mediated second messenger effects on K+ channels are dealt with elsewhere in this series. Recently, membrane-delimited pathways have been uncovered and an hypothesis proposed in which the alpha subunits of G proteins directly couple receptors to ionic channels, particularly K+ channels. While direct coupling has not been proven, the membrane-delimited nature has been established for specific G proteins and their specific K+ channel effectors.
MeSH term(s)	Animals ; GTP-Binding Proteins/metabolism ; Humans ; Potassium Channels/metabolism
Chemical Substances	Potassium Channels ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	1991-08
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	198499-8
ISSN	1573-6881 ; 0145-479X ; 0449-5705
ISSN (online)	1573-6881
ISSN	0145-479X ; 0449-5705
DOI	10.1007/bf00785808
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Article: Rapid desensitization of G protein-gated inwardly rectifying K(+) currents is determined by G protein cycle.

Leaney, Joanne L / Benians, Amy / Brown, Sean / Nobles, Muriel / Kelly, David / Tinker, Andrew

American journal of physiology. Cell physiology

2004 Volume 287, Issue 1, Page(s) C182–91

Abstract: Activation of G protein-gated inwardly rectifying K(+) (GIRK) channels, found in the brain, heart ... inhibitory postsynaptic potentials, slows the heart rate, and inhibits hormone release. During stimulation of G(i/o)-coupled ... of several G(i/o) G protein-coupled receptors (GPCRs) expressed in HEK-293 cells (adenosine A(1), adrenergic ...

Abstract	Activation of G protein-gated inwardly rectifying K(+) (GIRK) channels, found in the brain, heart, and endocrine tissue, leads to membrane hyperpolarization that generates neuronal inhibitory postsynaptic potentials, slows the heart rate, and inhibits hormone release. During stimulation of G(i/o)-coupled receptors and subsequent channel activation, it has been observed that the current desensitizes. In this study we examined mechanisms underlying fast desensitization of cloned heteromeric neuronal Kir3.1+3.2A and atrial Kir3.1+3.4 channels and also homomeric Kir3.0 currents in response to stimulation of several G(i/o) G protein-coupled receptors (GPCRs) expressed in HEK-293 cells (adenosine A(1), adrenergic alpha(2A), dopamine D(2S), M(4) muscarinic, and GABA(B1b/2) receptors). We found that all agonist-induced currents displayed a similar degree of desensitization except the adenosine A(1) receptor, which exhibits an additional desensitizing component. Using the nonhydrolyzable GTP analog guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS), we found that this is due to a receptor-dependent, G protein-independent process. Using Ca(2+) imaging we showed that desensitization is unlikely to be accounted for solely by phospholipase C activation and phosphatidylinositol 4,5-bisphosphate (PIP(2)) hydrolysis. We examined the contribution of the G protein cycle and found the following. First, agonist concentration is strongly correlated with degree of desensitization. Second, competitive inhibition of GDP/GTP exchange by using nonhydrolyzable guanosine 5'-O-(2-thiodiphosphate) (GDPbetaS) has two effects, a slowing of channel activation and an attenuation of the fast desensitization phenomenon. Finally, using specific Galpha subunits we showed that ternary complexes with fast activation rates display more prominent desensitization than those with slower activation kinetics. Together our data suggest that fast desensitization of GIRK currents is accounted for by the fundamental properties of the G protein cycle.
MeSH term(s)	Cell Line ; Electric Conductivity ; G Protein-Coupled Inwardly-Rectifying Potassium Channels ; GTP-Binding Protein alpha Subunits, Gq-G11/metabolism ; GTP-Binding Proteins/metabolism ; Humans ; Ion Channel Gating ; Potassium Channels/metabolism ; Potassium Channels, Inwardly Rectifying/metabolism ; Potassium Channels, Inwardly Rectifying/physiology ; Protein Isoforms/metabolism ; Receptors, Cell Surface/metabolism
Chemical Substances	G Protein-Coupled Inwardly-Rectifying Potassium Channels ; Potassium Channels ; Potassium Channels, Inwardly Rectifying ; Protein Isoforms ; Receptors, Cell Surface ; GTP-Binding Proteins (EC 3.6.1.-) ; GTP-Binding Protein alpha Subunits, Gq-G11 (EC 3.6.5.1)
Language	English
Publishing date	2004-03-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00540.2003
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Article: Differential phosphoinositide binding to components of the G protein-gated K+ channel.

Thomas, Alison M / Brown, Sean G / Leaney, Joanne L / Tinker, Andrew

The Journal of membrane biology

2006 Volume 211, Issue 1, Page(s) 43–53

Abstract: ... G protein-gated K(+) channels from the Kir3.0 family are involved in slowing the heart rate ...

Abstract	The regulation of ion channels and transporters by anionic phospholipids is currently very topical. G protein-gated K(+) channels from the Kir3.0 family are involved in slowing the heart rate, generating late inhibitory postsynaptic potentials and controlling hormone release from neuroendocrine cells. There is considerable functional precedent for the control of these channels by phosphatidylinositol 4,5-bisphosphate. In this study, we used a biochemical assay to investigate the lipid binding properties of Kir3.0 channel domains. We reveal a differential binding affinity to a range of phosphoinositides between the C termini of the Kir3.0 isoforms. Furthermore, the N terminus in addition to the C terminus of Kir3.4 is necessary to observe binding and is decreased by the mutations R72A, K195A and R196A but not K194A. Protein kinase C phosphorylation of the Kir3.1 C-terminal fusion protein decreases anionic phospholipid binding. The differential binding affinity has functional consequences as the inhibition of homomeric Kir3.1, occurring after M3 receptor activation, recovers over minutes while homomeric Kir3.2 does not.
MeSH term(s)	Amino Acid Sequence ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; G Protein-Coupled Inwardly-Rectifying Potassium Channels/genetics ; G Protein-Coupled Inwardly-Rectifying Potassium Channels/metabolism ; Humans ; Maltose-Binding Proteins ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphatidylinositols/metabolism ; Protein Binding/physiology ; Protein Kinase C/physiology ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism
Chemical Substances	Carrier Proteins ; G Protein-Coupled Inwardly-Rectifying Potassium Channels ; Maltose-Binding Proteins ; Phosphatidylinositols ; Recombinant Fusion Proteins ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2006-05
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3082-x
ISSN	1432-1424 ; 0022-2631
ISSN (online)	1432-1424
ISSN	0022-2631
DOI	10.1007/s00232-006-0014-5
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Article ; Online: The major G-quadruplex formed in the human platelet-derived growth factor receptor β promoter adopts a novel broken-strand structure in K+ solution.

Chen, Yuwei / Agrawal, Prashansa / Brown, Robert V / Hatzakis, Emmanuel / Hurley, Laurence / Yang, Danzhou

Journal of the American Chemical Society

2012 Volume 134, Issue 32, Page(s) 13220–13223

Abstract: ... of cancers and fibrotic disorders. DNA G-quadruplexes formed in the GC-rich nuclease hypersensitivity element ... we determined the major G-quadruplex formed in the PDGFR-β promoter. Instead of using four continuous runs ... with three or more guanines, this G-quadruplex adopts a novel folding with a broken G-strand to form ...

Abstract	Overexpression of platelet-derived growth factor receptor β (PDGFR-β) has been associated with cancers and vascular and fibrotic disorders. PDGFR-β has become an attractive target for the treatment of cancers and fibrotic disorders. DNA G-quadruplexes formed in the GC-rich nuclease hypersensitivity element of the human PDGFR-β gene promoter have been found to inhibit PDGFR-β transcriptional activity. Here we determined the major G-quadruplex formed in the PDGFR-β promoter. Instead of using four continuous runs with three or more guanines, this G-quadruplex adopts a novel folding with a broken G-strand to form a primarily parallel-stranded intramolecular structure with three 1 nucleotide (nt) double-chain-reversal loops and one additional lateral loop. The novel folding of the PDGFR-β promoter G-quadruplex emphasizes the robustness of parallel-stranded structural motifs with a 1 nt loop. Considering recent progress on G-quadruplexes formed in gene-promoter sequences, we suggest the 1 nt looped G(i)NG(j) motif may have been evolutionarily selected to serve as a stable foundation upon which the promoter G-quadruplexes can build. The novel folding of the PDGFR-β promoter G-quadruplex may be attractive for small-molecule drugs that specifically target this secondary structure and modulate PDGFR-β gene expression.
MeSH term(s)	Base Sequence ; Circular Dichroism ; G-Quadruplexes ; Humans ; Molecular Sequence Data ; Potassium/chemistry ; Promoter Regions, Genetic ; Protein Folding ; Receptor, Platelet-Derived Growth Factor beta/genetics ; Solutions
Chemical Substances	Solutions ; Receptor, Platelet-Derived Growth Factor beta (EC 2.7.10.1) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2012-08-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/ja305764d
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Article: Activation and inhibition of neuronal G protein-gated inwardly rectifying K(+) channels by P2Y nucleotide receptors.

Filippov, Alexander K / Fernández-Fernández, Jose M / Marsh, Stephen J / Simon, Joseph / Barnard, Eric A / Brown, David A

Molecular pharmacology

2004 Volume 66, Issue 3, Page(s) 468–477

Abstract: Neuronal signaling by G protein-coupled P2Y nucleotide receptors is not well characterized ... We studied here the coupling of different molecularly defined P2Y receptors to neuronal G protein-gated ... inward rectifier K(+) (GIRK) channels. Individual P2Y receptors were coexpressed with GIRK1+GIRK2 (Kir3.1 ...

Abstract	Neuronal signaling by G protein-coupled P2Y nucleotide receptors is not well characterized. We studied here the coupling of different molecularly defined P2Y receptors to neuronal G protein-gated inward rectifier K(+) (GIRK) channels. Individual P2Y receptors were coexpressed with GIRK1+GIRK2 (Kir3.1 + 3.2) channels by intranuclear plasmid injections into cultured rat sympathetic neurons. Currents were recorded using perforated-patch or whole-cell (disrupted patch) techniques, with similar results. P2Y(1) receptor stimulation with 2-methylthio ADP (2-MeSADP) induced activation of GIRK current (I(GIRK)) followed by inhibition. In contrast, stimulation of endogenous alpha(2)-adrenoceptors by norepinephrine produced stable activation without inhibition. P2Y(1)-mediated inhibition was also seen when 2-MeSADP was applied after I(GIRK) preactivation by norepinephrine or by expression of Gbeta(1)gamma(2) subunits. In contrast, stimulation of P2Y(4) receptors with UTP or P2Y(6) receptors with UDP produced very little I(GIRK) activation but significantly inhibited preactivated currents. Current activation was prevented by pertussis toxin (PTX) or after coexpression of the betagamma-scavenger transducin-Galpha.I(GIRK) inhibition by all three nucleotide receptors was insensitive to PTX and was significantly reduced after coexpression of RGS2 protein, known to inhibit G(q)alpha signaling. Inhibition was not affected 1) after coexpression of RGS11, which interferes with G(q)betagamma action; 2) after coexpression of phospholipase C (PLC) delta-Pleckstrin homology domain, which sequesters the membrane phospholipid phosphatidylinositol 4,5-bisphosphate; (3) after buffering intracellular Ca(2+) with 1,2-bis(2-aminiphenoxy)ethane-N,N,N',N'-tetraacetic acid acetoxymethyl ester (BAPTA-AM); and (4) after pretreatment with the protein kinase C inhibitor 3-[1-[3-(dimethylaminopropyl]-1H-indol-3-yl]-4-(1H-indol-3-yl)-1H-pyrrole-2,5-dione monohydrochloride (GF 109203X). We conclude that activation of I(GIRK) by P2Y receptors is mediated by G(i/o)betagamma, whereas I(GIRK) inhibition is mediated by G(q)alpha. These effects may provide a mechanism for P2Y-modulation of neuronal excitability.
MeSH term(s)	Animals ; Calcium/metabolism ; Cells, Cultured ; G Protein-Coupled Inwardly-Rectifying Potassium Channels ; GTP-Binding Proteins/metabolism ; Male ; Neurons/metabolism ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Potassium Channels/metabolism ; Potassium Channels, Inwardly Rectifying ; Protein Kinase C/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Purinergic P2/physiology ; Receptors, Purinergic P2Y1 ; Type C Phospholipases/metabolism
Chemical Substances	G Protein-Coupled Inwardly-Rectifying Potassium Channels ; P2ry1 protein, rat ; Phosphatidylinositol 4,5-Diphosphate ; Potassium Channels ; Potassium Channels, Inwardly Rectifying ; Receptors, Purinergic P2 ; Receptors, Purinergic P2Y1 ; purinoceptor P2Y4 ; purinoceptor P2Y6 ; Protein Kinase C (EC 2.7.11.13) ; Type C Phospholipases (EC 3.1.4.-) ; GTP-Binding Proteins (EC 3.6.1.-) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2004-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	124034-1
ISSN	1521-0111 ; 0026-895X
ISSN (online)	1521-0111
ISSN	0026-895X
DOI	10.1124/mol.66.3.
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Article: Differential Phosphoinositide Binding to Components of the G Protein-Gated K⁺ Channel

Thomas, Alison M / Brown, Sean G / Leaney, Joanne L / Tinker, Andrew

Journal of membrane biology. 2006 May, v. 211, no. 1

2006

Abstract: ... G protein-gated K⁺ channels from the Kir3.0 family are involved in slowing the heart rate ...

Abstract	The regulation of ion channels and transporters by anionic phospholipids is currently very topical. G protein-gated K⁺ channels from the Kir3.0 family are involved in slowing the heart rate, generating late inhibitory postsynaptic potentials and controlling hormone release from neuroendocrine cells. There is considerable functional precedent for the control of these channels by phosphatidylinositol 4,5-bisphosphate. In this study, we used a biochemical assay to investigate the lipid binding properties of Kir3.0 channel domains. We reveal a differential binding affinity to a range of phosphoinositides between the C termini of the Kir3.0 isoforms. Furthermore, the N terminus in addition to the C terminus of Kir3.4 is necessary to observe binding and is decreased by the mutations R72A, K195A and R196A but not K194A. Protein kinase C phosphorylation of the Kir3.1 C-terminal fusion protein decreases anionic phospholipid binding. The differential binding affinity has functional consequences as the inhibition of homomeric Kir3.1, occurring after M3 receptor activation, recovers over minutes while homomeric Kir3.2 does not.
Language	English
Dates of publication	2006-05
Size	p. 43-53.
Publisher	Springer-Verlag
Publishing place	New York
Document type	Article
ZDB-ID	3082-x
ISSN	1432-1424 ; 0022-2631
ISSN (online)	1432-1424
ISSN	0022-2631
DOI	10.1007/s00232-006-0014-5
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Article: G protein opening of K+ channels.

Birnbaumer, L / Brown, A M

Nature

1987 Volume 327, Issue 6117, Page(s) 21–22

MeSH term(s)	Animals ; Chick Embryo ; GTP-Binding Proteins/isolation & purification ; GTP-Binding Proteins/physiology ; Ion Channels/metabolism ; Mammals ; Myocardium/analysis ; Receptors, Muscarinic/physiology
Chemical Substances	Ion Channels ; Receptors, Muscarinic ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	1987-05
Publishing country	England
Document type	Letter
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/327021a0
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Article: The Major G-Quadruplex Formed in the Human Platelet-Derived Growth Factor Receptor Î² Promoter Adopts a Novel Broken-Strand Structure in K+ Solution

Chen, Yuwei / Agrawal Prashansa / Brown Robert V / Hatzakis Emmanuel / Hurley Laurence / Yang Danzhou

Journal of the American Chemical Society. 2012 Aug. 15, v. 134, no. 32

2012

Abstract: ... of cancers and fibrotic disorders. DNA G-quadruplexes formed in the GC-rich nuclease hypersensitivity element ... we determined the major G-quadruplex formed in the PDGFR-Î² promoter. Instead of using four continuous runs ... with three or more guanines, this G-quadruplex adopts a novel folding with a broken G-strand to form ...

Abstract	Overexpression of platelet-derived growth factor receptor Î² (PDGFR-Î²) has been associated with cancers and vascular and fibrotic disorders. PDGFR-Î² has become an attractive target for the treatment of cancers and fibrotic disorders. DNA G-quadruplexes formed in the GC-rich nuclease hypersensitivity element of the human PDGFR-Î² gene promoter have been found to inhibit PDGFR-Î² transcriptional activity. Here we determined the major G-quadruplex formed in the PDGFR-Î² promoter. Instead of using four continuous runs with three or more guanines, this G-quadruplex adopts a novel folding with a broken G-strand to form a primarily parallel-stranded intramolecular structure with three 1 nucleotide (nt) double-chain-reversal loops and one additional lateral loop. The novel folding of the PDGFR-Î² promoter G-quadruplex emphasizes the robustness of parallel-stranded structural motifs with a 1 nt loop. Considering recent progress on G-quadruplexes formed in gene-promoter sequences, we suggest the 1 nt looped Gáµ¢NGâ±¼ motif may have been evolutionarily selected to serve as a stable foundation upon which the promoter G-quadruplexes can build. The novel folding of the PDGFR-Î² promoter G-quadruplex may be attractive for small-molecule drugs that specifically target this secondary structure and modulate PDGFR-Î² gene expression.
Keywords	DNA ; drugs ; gene expression ; genes ; humans ; hypersensitivity ; neoplasms ; platelet-derived growth factor receptors ; potassium ; transcription (genetics)
Language	English
Dates of publication	2012-0815
Size	p. 13220-13223.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021%2Fja305764d
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Article: Gating of atrial muscarinic K+ channels by G proteins.

Brown, A M / Yatani, A / Codina, J / Birnbaumer, L

Progress in clinical and biological research

1990 Volume 334, Page(s) 303–312

MeSH term(s)	Enzyme Activation ; Erythrocyte Membrane/metabolism ; Erythrocyte Membrane/physiology ; GTP-Binding Proteins/immunology ; GTP-Binding Proteins/physiology ; Gene Expression ; Humans ; In Vitro Techniques ; Ion Channel Gating/physiology ; Myocardium/metabolism ; Potassium Channels/physiology ; Protein Kinase C/physiology ; Receptors, Muscarinic/physiology ; Recombinant Proteins ; Signal Transduction
Chemical Substances	Potassium Channels ; Receptors, Muscarinic ; Recombinant Proteins ; Protein Kinase C (EC 2.7.11.13) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	1990
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ISSN	0361-7742
ISSN	0361-7742
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